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Plant and Cell Physiology, 2003, Vol. 44, No. 2 173-182
© 2003 Oxford University Press

Fusion with HDEL Protects Cell Wall Invertase from Early Degradation when N-glycosylation is Inhibited

Sophie Pagny, Lise-Anne Denmat-Ouisse1, Véronique Gomord and Loïc Faye2

CNRS-UMR 6037, IFRMP 23, Université de Rouen, F-76 821 Mont Saint Aignan, France

Previous data obtained in different suspension-cultured plant cells have clearly illustrated that N-glycans are absolutely required for transport of glycoproteins to the extracellular compartment, regardless of their oligosaccharide structure [see Lerouge et al. (1998) Plant Mol. Biol. 38: 31 for review]. In the present study the role of N-glycosylation in the transport of glycoproteins to the cell surface was studied in BY2 tobacco cells using both endogenous and recombinant cell wall invertases as markers. When synthesized without their N-glycans, both invertases were very rapidly degraded. This degradation did not occur in an acidic compartment and was brefeldin A-insensitive. Therefore, it most probably represents a pre-Golgi event. However, the low efficiency of specific inhibitors did not favor a strong contribution of proteasomes in this proteolysis. In contrast, addition of a C-terminal His-Asp-Glu-Leu (HDEL) extension prevented arrival of these non-glycosylated glycoproteins in the compartment where they are degraded. These results argue for the presence of an endoplasmic reticulum (ER) domain specialized in protein degradation. Consistent with our results and the well-known stabilization of recombinant proteins retained in the ER, the addition of an ER retention signal to a protein would prevent its targeting to an ER domain devoted to degradation.

1 Present address: Laboratoire de Biochimie des Transports Cellulaires, CNRS UMR 8619, Universite Paris XI, F-91405 Orsay cedex, France.

2 Corresponding author: E-mail, lfaye{at}crihan.fr; Fax, +33-2-35-14-67-87.


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